2.7.7.19: polynucleotide adenylyltransferase
This is an abbreviated version!
For detailed information about polynucleotide adenylyltransferase, go to the full flat file.
Word Map on EC 2.7.7.19
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2.7.7.19
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polyadenylation
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polymerases
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pre-mrnas
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phosphorylase
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exosome
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rna-binding
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vaccinia
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trna
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oligoa
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helicase
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tramp
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aauaaa
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deadenylation
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polya-binding
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pnpase
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dna-dependent
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meiotic
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noncanonical
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exonuclease
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3'-terminal
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cordycepin
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oligoadenylation
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exoribonucleases
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polyu
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drug development
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endoribonuclease
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medicine
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snornas
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non-templated
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cca-adding
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hfq
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polya-specific
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deadenylase
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biotechnology
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polya-tailed
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snrnp
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pabpn1
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degradosome
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exonucleolytic
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3'-deoxyadenosine
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pancreatitis-associated
- 2.7.7.19
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polyadenylation
- polymerases
- pre-mrnas
- phosphorylase
-
exosome
-
rna-binding
- vaccinia
- trna
-
oligoa
- helicase
-
tramp
-
aauaaa
-
deadenylation
-
polya-binding
- pnpase
-
dna-dependent
-
meiotic
-
noncanonical
-
exonuclease
-
3'-terminal
- cordycepin
-
oligoadenylation
- exoribonucleases
- polyu
- drug development
-
endoribonuclease
- medicine
- snornas
-
non-templated
-
cca-adding
- hfq
-
polya-specific
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deadenylase
- biotechnology
-
polya-tailed
-
snrnp
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pabpn1
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degradosome
-
exonucleolytic
- 3'-deoxyadenosine
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pancreatitis-associated
Reaction
Synonyms
AAS, adenosine triphosphate:ribonucleic acid adenylyltransferase, AMP polynucleotidylexotransferase, ATP-polynucleotide adenylyltransferase, ATP:polynucleotidylexotransferase, CC-adding enzyme, Cid1, Cid14, FAM46A, FAM46B, FAM46C, FAM46D, germline development 2, GLD-2, GLD2, GLD4, Hs2, MTPAP, neo-PAP, non-canonical poly(A) RNA polymerase PAPD7, NTP polymerase, nuclear poly(A) polymerase 1, nuclear speckle targeted PIPKIalpha regulated-poly(A) polymerase, nucleotidyltransferase, polyadenylate, PAP, PAP I, Pap II, PAP1, Pap1p, PAPalpha, PAPbeta, PapD1, PapD5, PAPD7, PAPgamma, PAPOLA, PAPOLB/TPAP, PAPOLG, PAPS1, PAPS2, PAPS4, PcnB, pcnB2, pcnB2 aq_2158, poly A polymerase, poly(A) hydrolase, poly(A) polymerase, poly(A) polymerase gamma, poly(A) polymerase I, poly(A) polymerase II, poly(A) RNA polymerase protein 1, poly(A) synthetase, poly(A)-polymerase, poly(A)polymerase I, polyA polymerase, polyadenylate nucleotidyltransferase, polyadenylate polymerase, polyadenylate synthetase, polyadenylic acid polymerase, polyadenylic polymerase, poly[A] polymerase beta, RNA adenylating enzyme, RNA formation factors, PF1, RNA poly(A) polymerase, Star-PAP, Tb927.3.3160, Tb927.7.3780, terminal riboadenylate transferase, Tpap, Trf5, Trf5p, TUT1, TUTase1, VP55, Wisp, yPAP, ZCCHC6
ECTree
2.7.7.19 polynucleotide adenylyltransferaseAdvanced search results
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results (Engineering
Engineering on EC 2.7.7.19 - polynucleotide adenylyltransferase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
C36S/C118V/A152C/C160S/C197S/C257S/C293S/C204V
introduction of a Cys residue in a mutant lacking all endogenous Cys residues. Mutant achieves maximum specific disulfide cross-linking efficiency. The resulting construct is active and, when mixed with a chemically modified RNA, yields crystals of an enzyme-RNA complex
C36S/C118V/C160S/C197S/C257S/C293S/C204V
mutation of all seven endogenous cysteine residues. Mutant is able to bind RNA at a level similar to that of wild-type, but no longer forms nonspecific disulfide cross-links with the modified RNA
N202A
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high Km value for RNA, strong reduction of catalytic efficiency, incorporates etheno-ATP and N1-methyl-ATP better than wild-type, but incorporates N6-methyl-ATP poorly
T317G
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increase in Km for ATP, tolerates etheno-ATP and GTP, rejects N6-methyl-ATP
V247R
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kcat for ATP is reduced 2000-fold, strong reduction of catalytic efficiency
D170A
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diphosphate release equivalent to AMP production, 5-30% of wild type activity
D170P
D212A
mutant enzyme forms specifically incorporated A-residues with a fidelity comparable to that of the wild type enzyme
D214A
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diphosphate release equivalent to AMP production, 5-30% of wild type activity
D214P
D88A
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diphosphate release equivalent to AMP production, 5-30% of wild type activity
D88P
D90A
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diphosphate release equivalent to AMP production, 5-30% of wild type activity
D90P
E211A
mutant enzyme forms specifically incorporated A-residues with a fidelity comparable to that of the wild type enzyme
R215A
the mutation leads to a dramatic loss in nucleotide specificity and the formation of poly(N) tails
D237N
loss of activity. A heterodimer in which one monomer is active and the other is not retains activity
K112E
disruption of a a continuous positively charged surface formed upon dimerization, decrease in activity
K76E/K80E/K81E
disruption of a a continuous positively charged surface formed upon dimerization, decrease in activity
D124A
the mutant shows strongly reduced activity compared to the wild type enzyme
D126A
the mutant shows strongly reduced activity compared to the wild type enzyme
D325A
mutation of one of the conserved Asp residues in the active site, complete loss of activity. The mutant protein gives better quality crystals than the wild-type enzyme
E200A
the mutant shows strongly reduced activity compared to the wild type enzyme
G107A
the mutant shows strongly reduced activity compared to the wild type enzyme
H259A/K260A/I261A/H294A/F295A/P297A
mutations simultaneously disrupt both areas of contact in the dimer interface, mutant is a stable monomer in solution, complete loss of activity
H294A/F295A/P297A
mutation in helix alphaE, mutant exists in a monomer-dimer equilibrium
K560E
mutation in the C-terminal basic motif. About 20% of wild-type activity
S108A
the mutant shows strongly reduced activity compared to the wild type enzyme
Y221A/F222A
mutation in helix alphaB, mutant exists in a monomer-dimer equilibrium
D154A
K215A
N189A
N226A
V498Y/C485R
the mutant is unable to bind Fip1 but retains full polymerase activity
Y224F
Y224S
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12-fold increase in the Km for oligo(A)14 in comparison with wild-type enzyme, 2.8-3.6-fold decrease in Vmax
additional information
D170P
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diphosphate release equivalent to AMP production, 5-30% of wild type activity
D214P
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diphosphate release equivalent to AMP production, 5-30% of wild type activity
D88P
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diphosphate release equivalent to AMP production, 5-30% of wild type activity
D90P
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diphosphate release equivalent to AMP production, 5-30% of wild type activity
D154A
crystallization data, closed conformation with extensive interactions between substrates and all three polymerase domains
D154A
the mutant has a nearly identical melting temperature as wild type PAP
K215A
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74- and 56-fold increase in the Km for oligo(A)14 in comparison with wild-type enzyme, 2.8-3.6-fold decrease in Vmax
K215A
the mutant has a nearly identical melting temperature as wild type PAP
N189A
residue bridges the N and middle domains in the closed state
N189A
the mutant has a nearly identical melting temperature as wild type PAP
N226A
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74- and 56-fold increase in the Km for oligo(A)14 in comparison with wild-type enzyme
N226A
mutation affects the equilibrium between the open- and closed-domain forms of the enzyme
N226A
the mutant has a nearly identical melting temperature as wild type PAP
Y224F
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30-fold increase in the Km for oligo(A)14 in comparison with wild-type enzyme, 2.8-3.6-fold decrease in Vmax
Y224F
mutation affects the equilibrium between the open- and closed-domain forms of the enzyme
Y224F
altered melting temperature (44°C) compared to the wild type enzyme
additional information
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chimeras of CCA-adding enzyme and PAP were constructed
additional information
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enzyme knockout mutant, the mRNA levels of bolA, which is induced in response to many forms of stress, are reduced 2.5fold in stationary phase. Absence of enzyme enhances the RssB-mediated deltaS proteolysis specifically in starved cells
additional information
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enzyme PAP I variant with C-terminal His-tag can be phosphorylated both in vivo and in vitro. In vivo phosphorylation impairs activity of the enzyme
additional information
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reengineering of enzyme in order to function as (UG) adding enzyme. Double- and triple-mutants in residues 211, 212, 215 add 570 G residues to oligoA15 substrate
additional information
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hmtPAP knockdown mutant cells show decreased steady state levels of mtDNA-encoded proteins as well as deficient mitochondrial activities such as oxygen consumption rate
additional information
deletion variant of the C-terminal part lacking amino acids 369-551. Whereas the C terminus binds to RNA, the deletion variant shows no shift of the RNA in EMSA experiments
additional information
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deletion variant of the C-terminal part lacking amino acids 369-551. Whereas the C terminus binds to RNA, the deletion variant shows no shift of the RNA in EMSA experiments
additional information
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GLD-2 disruption does not affect the poly(A) tail elongation in oocytes
additional information
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the un-17 mutant carries a temperature-sensitive mutation in the gene encoding PAP
additional information
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deletion of C-terminal 31 amino acids has no effect, deletion of C-terminal 67 amino acids affects RNA binding, deletion of N-terminal 18 amino acids eliminates specific activity
additional information
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mutation of bovine residue N202 (equivalent to yeast N189) to alanine has essentially no effect on the apparent Km for ATP, but has a pronounced effect on the apparent Vmax, suggesting that this residue is particularly important in the recognition of the adenine of ATP
additional information
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strain lacking the Rrp6p component of the nuclear exosome accumulate polyadenylated forms of different ribosomal RNA precursors. This polyadenylation is reduced in strains lacking polynucleotide adenylyltransferase Trf5p and enhanced in strains overexpressing Trf5p
